Lesson eLearning

Insulin is a polypeptide hormone consisting of two chains A and B linked by two inter‑chain disulfide bonds and one intra‑chain bond in the A chain. Explain how reduction of these disulfide bonds affects insulin’s ability to bind to its receptor. Include a brief description of the structural consequence and the functional outcome.

hard 5 marks Class 12 · Chemistry · Biomolecules
Answer
Reduction breaks disulfide bridges, unfolding insulin and abolishing its receptor binding ability.

The correct answer is Reduction breaks disulfide bridges, unfolding insulin and abolishing its receptor binding ability. — Conclude that the unfolded insulin cannot adopt the conformation required for high‑affinity receptor binding, thus losing its biological activity.

Step-by-step solution

  1. Describe insulin’s native structure: two chains linked by disulfide bonds that stabilize its folded conformation.
  2. Explain that reducing agents (e.g., dithiothreitol) cleave disulfide bridges, converting –S–S– bonds to free –SH groups.
  3. State that breaking these bonds disrupts the tertiary structure, leading to an unfolded or partially folded protein.
  4. Conclude that the unfolded insulin cannot adopt the conformation required for high‑affinity receptor binding, thus losing its biological activity.
Common mistake: Believing reduction has no effect on insulin’s function

Concept tested: Disulfide bridges stabilize protein folding

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